Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors

Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L (1998)
FEBS LETTERS 421(1): 80-82.

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Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 1998;421(1):80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., & Moroder, L. (1998). Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS, 421(1), 80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., and Moroder, L. (1998). Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS 421, 80-82.
Schaschke, N., et al., 1998. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS, 421(1), p 80-82.
N. Schaschke, et al., “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”, FEBS LETTERS, vol. 421, 1998, pp. 80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., Moroder, L.: Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 421, 80-82 (1998).
Schaschke, Norbert, Assfalg-Machleidt, I, Machleidt, W, and Moroder, L. “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”. FEBS LETTERS 421.1 (1998): 80-82.
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15 Citations in Europe PMC

Data provided by Europe PubMed Central.

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Epoxysuccinyl peptide-derived cathepsin B inhibitors: modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin.
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Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections.
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Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.
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Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?
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